Weitere Antikörper gegen Elastin Interaktionspartner

Cow (Bovine) Elastin (ELN) Interaktionspartner

we show on the molecular level that elastin formation involves random cross-linking of tropoelastin monomers resulting in an unordered network, an unexpected finding compared with previous assumptions of an overall beaded structure

Data suggest that cross-linking involving desmosine and isodesmosine residues in bovine elastin and human tropoelastin contributes to long-term stability of these proteins.

Immersing elastin in various glycerol-water mixtures, we observe at room temperature that the protein mobility is higher for lower glycerol fractions in the solvent and, thus, lower solvent viscosity.

domain 36 of tropoelastin contributes to the binding to fibrillin-1 and microfibril-associated glycoprotein through two cysteine residues and Lysine-Arginine-Lysine-Arginine sequence, resulting in the promotion of elastic fiber assembly.

Biaxial force-controlled experiments were used to quantify regional variations in the anisotropy and nonlinearity of elastin isolated from bovine aortic tissues proximal and distal to the heart.

the mechanism by which ONOO(-) prevents cell binding to TE is by introducing negatively charged sulfonic acid residues near the positively charged cluster.

In cases of vascular calcification, the decreased expression of tropoelastin may be partially responsible for decreased vascular elasticity and also for the decreased formation of new elastic fibers.

tropoelastin has domains that mediate elastin deposition in vitro and in vivo

TE can associate with elastic fiber components in the absence of live cells through a process that does not depend on crosslink formation

B-Myb represses SMC elastin gene expression and cyclin A plays a role in the developmental regulation of elastin gene expression in the aorta

self-association and oxidation by lysyl oxidase precedes tropoelastin deposition onto microfibrils; the entire molecule of tropoelastin is required for this following maturation process

analysis of functional inactivation of the tropoelastin carboxy-terminal domain in cross-linked elastin

Human Elastin (ELN) Interaktionspartner

The majority of familial SVAS patients appear to carry ELN mutations, which strongly indicates that elastin is the most important causative gene for SVAS. The frequency of intragenic deletions highlights the need for quantitative tests to analyze ELN for efficient genetic diagnosis of SVAS.

In conclusion, our results support the view that lysyl oxidase (LOX) and tropoelastin are present on the cell surface and suggests the possibility that lysine oxidation by LOX precedes tropoelastin deposition onto microfibrils.

Elastin degradation was correlated with age in COPD patients, smoker controls, and non-smoker controls. The correlation was weaker in the smoker control group compared with the never-smoker control or COPD group.

The aim was to examine if the serum concentrations of elastin-related proteins correlate to signs of cardiovascular diseases in patients with Diabetes mellitus type 2.

There is evidence that the ELN variant INT20 1315T > C is implicated in the development of intracranial aneurysm.

Direct gene sequencing of ELN confirmed the diagnosis showing a previously undescribed c.2156del (p.Gly719Glufs*36) mutation in exon 30 of ELN gene. This mutation results in a shift of the reading frame.

Here we report a second adult Williams-Beuren syndrome (WBS)patient with emphysema where the diagnosis of WBS was established subsequent to the discovery of severe bullous emphysema. Haploinsufficiency of ELN likely contributed to this pulmonary manifestation of WBS.

the study contributes to a better understanding of the correlation between genotypic and elastin-related phenotypic features of Williams-Beuren syndrome patients

We herein report the case of a Japanese female patient presenting with multiple arteriopathy including moyamoya disease, a tortuosity of abdominal arteries and pulmonary hypertension due to peripheral pulmonary artery stenosis. This case suggests the possible progression of cerebral arteriopathy including moyamoya disease in patients with elastin mutations

These results indicate that elastin neoepitopes generated by the same proteases but at different amino acid sites provide different tissue-related information depending on the disease in question.

Mouse (Murine) Elastin (ELN) Interaktionspartner

Data (including data from studies in mutant mice and cells from such mice) suggest that elastin-derived peptides are involved in regulation of lipid storage in hepatocytes; thus, elastin-derived peptides may play role in development and progression of non-alcoholic fatty liver.

Data suggest that expression of elastin in uterus, vagina, and bladder is down-regulated both in naturally aging mice and in mouse model of accelerated ovarian aging; such down-regulation may lead to pelvic floor disorders.

tested the hypothesis that adhesive strength varies with atherosclerotic plaque composition of collagen and elastin in apoE and MMP12 knock outs

Data show that tropoelastin staining was relatively weak in the ligamentum flavum from E15 through P0, P7 was the first stage that staining intensity was observed to be substantially stronger, intensity remained relatively high until P35.

Pig (Porcine) Elastin (ELN) Interaktionspartner

The elastic fibers are under tension and impart an intrinsic compressive stress on the collagen.

A biomechanical model of the common carotid artery predicts that the majority of elastin is in-series with vascular smooth muscle (74 +/-8%), thus only about one-fourth of elastin acts in parallel to the vascular smooth muscle within the arterial wall.

Elastin (ELN) Antigen-Profil

Beschreibung des Gens

This gene encodes a protein that is one of the two components of elastic fibers. The encoded protein is rich in hydrophobic amino acids such as glycine and proline, which form mobile hydrophobic regions bounded by crosslinks between lysine residues. Deletions and mutations in this gene are associated with supravalvular aortic stenosis (SVAS) and autosomal dominant cutis laxa. Multiple transcript variants encoding different isoforms have been found for this gene.